2002
Exclusive Interaction of the 15.5 kD Protein with the Terminal Box C/D Motif of a Methylation Guide snoRNP
Szewczak LB, DeGregorio SJ, Strobel SA, Steitz JA. Exclusive Interaction of the 15.5 kD Protein with the Terminal Box C/D Motif of a Methylation Guide snoRNP. Cell Chemical Biology 2002, 9: 1095-1107. PMID: 12401494, DOI: 10.1016/s1074-5521(02)00239-9.Peer-Reviewed Original ResearchConceptsBox C/D motifKD proteinD motifBox C/D snoRNAsBox C/D snoRNPsSite-specific methylationSpliceosomal RNAsDeleterious substitutionsD snoRNAsD snoRNPsBox DExclusive interactionsInteraction sitesXenopus oocytesSnoRNPsProteinMotifSnoRNAsVivoMethylationA89Single interaction siteRNAExocyclic amineOocytes
1997
Identification of HuR as a protein implicated in AUUUA‐mediated mRNA decay
Myer V, Fan X, Steitz J. Identification of HuR as a protein implicated in AUUUA‐mediated mRNA decay. The EMBO Journal 1997, 16: 2130-2139. PMID: 9155038, PMCID: PMC1169815, DOI: 10.1093/emboj/16.8.2130.Peer-Reviewed Original ResearchMeSH Keywords3T3 CellsAmino Acid SequenceAnimalsAntigens, SurfaceBase CompositionCell ExtractsCross-Linking ReagentsELAV ProteinsELAV-Like Protein 1Gene Expression RegulationHeLa CellsHumansMiceMolecular Sequence DataMolecular WeightRegulatory Sequences, Nucleic AcidRNA-Binding ProteinsRNA, MessengerUltraviolet RaysConceptsAU-rich elementsMRNA decayUntranslated regionRNA-binding specificityARE-binding proteinsHeLa nuclear extractsGene familyMRNA degradationNuclear extractsEssential signalMessenger RNAProteinSequence's abilityHuRAUUUARapid degradationCritical roleHuR.RNAMachineryMRNADegradationRegulationSubsequent analysisExpression
1993
A base-pairing interaction between U2 and U6 small nuclear RNAs occurs in > 150S complexes in HeLa cell extracts: implications for the spliceosome assembly pathway.
Wassarman DA, Steitz JA. A base-pairing interaction between U2 and U6 small nuclear RNAs occurs in > 150S complexes in HeLa cell extracts: implications for the spliceosome assembly pathway. Proceedings Of The National Academy Of Sciences Of The United States Of America 1993, 90: 7139-7143. PMID: 8346227, PMCID: PMC47091, DOI: 10.1073/pnas.90.15.7139.Peer-Reviewed Original ResearchConceptsU6 small nuclear RNASmall nuclear RNAS100 extractsNuclear RNASer/Arg-rich (SR) proteinsBase pairingNuclear extractsLarge complexesArg-rich proteinsPre-RNA splicingSpliceosome assembly pathwayHeLa cell extractsHeLa nuclear extractsBase-pairing interactionsBase pair formsPossible functional relationshipRibonucleoprotein complexesSpliceosome complexMammalian cellsAssembly pathwaySplicing substratePsoralen crosslinkingGlycerol gradientsCell extractsSplicing
1991
Structural analyses of the 7SK ribonucleoprotein (RNP), the most abundant human small RNP of unknown function.
Wassarman DA, Steitz JA. Structural analyses of the 7SK ribonucleoprotein (RNP), the most abundant human small RNP of unknown function. Molecular And Cellular Biology 1991, 11: 3432-3445. PMID: 1646389, PMCID: PMC361072, DOI: 10.1128/mcb.11.7.3432.Peer-Reviewed Original Research
1989
The mammalian analogue of the yeast PRP8 splicing protein is present in the U4/5/6 small nuclear ribonucleoprotein particle and the spliceosome.
Pinto AL, Steitz JA. The mammalian analogue of the yeast PRP8 splicing protein is present in the U4/5/6 small nuclear ribonucleoprotein particle and the spliceosome. Proceedings Of The National Academy Of Sciences Of The United States Of America 1989, 86: 8742-8746. PMID: 2479028, PMCID: PMC298364, DOI: 10.1073/pnas.86.22.8742.Peer-Reviewed Original ResearchConceptsSmall nuclear ribonucleoproteinU5 small nuclear ribonucleoproteinHeLa cell nuclear extractsSmall nuclear ribonucleoprotein particleCell nuclear extractsAnti-trimethylguanosine antibodyNuclear ribonucleoprotein particleAffinity-purified spliceosomesSplicing proteinsMammalian proteinsYeast proteinsSnRNP complexMRNA splicingSplicing extractsRibonucleoprotein particleNuclear ribonucleoproteinMammalian analogueNuclear extractsSm classGradient fractionationSm epitopesProteinSpliceosomeProtein reactivePrp8
1984
The structure of mammalian small nuclear ribonucleoproteins. Identification of multiple protein components reactive with anti-(U1)ribonucleoprotein and anti-Sm autoantibodies.
Pettersson I, Hinterberger M, Mimori T, Gottlieb E, Steitz JA. The structure of mammalian small nuclear ribonucleoproteins. Identification of multiple protein components reactive with anti-(U1)ribonucleoprotein and anti-Sm autoantibodies. Journal Of Biological Chemistry 1984, 259: 5907-5914. PMID: 6232278, DOI: 10.1016/s0021-9258(18)91101-4.Peer-Reviewed Original ResearchConceptsSm small nuclear ribonucleoproteinsSmall nuclear ribonucleoproteinNuclear ribonucleoproteinProtein componentsAnti-Sm patient seraMultiple protein componentsSnRNP proteinsU6 RNAMammalian cellsDistinct polypeptidesAnti-Sm monoclonal antibodyRNA immunoprecipitationAnti-Sm autoantibodiesSnRNP polypeptidesProtein compositionSnRNP particlesProtein BMonoclonal antibodiesRibonucleoproteinIntriguing questionPolypeptideProteinBlot resultsMouse monoclonal antibodyEntire collectionThe Ro small cytoplasmic ribonucleoproteins: identification of the antigenic protein and its binding site on the Ro RNAs.
Wolin SL, Steitz JA. The Ro small cytoplasmic ribonucleoproteins: identification of the antigenic protein and its binding site on the Ro RNAs. Proceedings Of The National Academy Of Sciences Of The United States Of America 1984, 81: 1996-2000. PMID: 6201849, PMCID: PMC345423, DOI: 10.1073/pnas.81.7.1996.Peer-Reviewed Original ResearchConceptsRibonucleoprotein particleHeLa cellsSmall cytoplasmic RNARibonuclease protection experimentsSmall ribonucleoprotein particlesSmall cytoplasmic ribonucleoproteinsHuman HeLa cellsCytoplasmic ribonucleoproteinMammalian speciesCytoplasmic RNARNA sequencesMajor proteinsRo RNAsProtection experimentsRo proteinPossible functionsBase pairsIdentical base pairsRNAProteinSystemic lupus erythematosusAntigenic proteinsAntigenic polypeptidesRo antibodiesLupus erythematosus
1983
Sequential association of nucleolar 7-2 RNA with two different autoantigens.
Hashimoto C, Steitz JA. Sequential association of nucleolar 7-2 RNA with two different autoantigens. Journal Of Biological Chemistry 1983, 258: 1379-1382. PMID: 6185483, DOI: 10.1016/s0021-9258(18)32990-9.Peer-Reviewed Original ResearchSmall ribonucleoproteins from eukaryotes: structures and roles in RNA biogenesis.
Steitz JA, Wolin SL, Rinke J, Pettersson I, Mount SM, Lerner EA, Hinterberger M, Gottlieb E. Small ribonucleoproteins from eukaryotes: structures and roles in RNA biogenesis. Cold Spring Harbor Symposia On Quantitative Biology 1983, 47 Pt 2: 893-900. PMID: 6222869, DOI: 10.1101/sqb.1983.047.01.103.Peer-Reviewed Original Research
1981
A small nuclear ribonucleoprotein is required for splicing of adenoviral early RNA sequences.
Yang VW, Lerner MR, Steitz JA, Flint SJ. A small nuclear ribonucleoprotein is required for splicing of adenoviral early RNA sequences. Proceedings Of The National Academy Of Sciences Of The United States Of America 1981, 78: 1371-1375. PMID: 6940164, PMCID: PMC319132, DOI: 10.1073/pnas.78.3.1371.Peer-Reviewed Original Research
1980
Are snRNPs involved in splicing?
Lerner M, Boyle J, Mount S, Wolin S, Steitz J. Are snRNPs involved in splicing? Nature 1980, 283: 220-224. PMID: 7350545, DOI: 10.1038/283220a0.Peer-Reviewed Original ResearchConceptsSmall nuclear RNA speciesProminent nuclear proteinsRNA-protein complexesSmall RNA moleculesSmall nuclear ribonucleoproteinNuclear RNA speciesSnRNA speciesSnRNAs U1RNA speciesU6 RNASnRNA moleculesNuclear proteinsNuclear ribonucleoproteinNucleotide sequenceU1 RNARNA moleculesSnRNPsExtensive complementaritySplice junctionsNuclear locationLines of evidenceAnti-Sm seraCell nucleiHnRNA moleculesMouse Ehrlich
1979
Antibodies to small nuclear RNAs complexed with proteins are produced by patients with systemic lupus erythematosus
Lerner M, Steitz J. Antibodies to small nuclear RNAs complexed with proteins are produced by patients with systemic lupus erythematosus. Proceedings Of The National Academy Of Sciences Of The United States Of America 1979, 76: 5495-5499. PMID: 316537, PMCID: PMC411675, DOI: 10.1073/pnas.76.11.5495.Peer-Reviewed Original ResearchMeSH KeywordsAntibodies, AntinuclearAntibody SpecificityHumansLupus Erythematosus, SystemicMolecular WeightNucleoproteinsRibonucleoproteinsRNAConceptsSmall nuclear RNA moleculesNuclear extractsMouse Ehrlich ascites cellsSmall nuclear RNANuclear RNA moleculesSmall nuclear ribonucleoproteinNuclear RNP particlesMammalian nucleiVertebrate speciesNuclear RNANuclear ribonucleoproteinRNA moleculesSystemic lupus erythematosusDifferent polypeptidesEhrlich ascites cellsIdentical complementSpecific proteinsMajor polypeptidesRNP particlesMolecular identityPossible functionsNuclear processesNuclear RNPAnti-Sm seraVirtue of associationTandem promoters direct E. coli ribosomal RNA synthesis
Young R, Steitz J. Tandem promoters direct E. coli ribosomal RNA synthesis. Cell 1979, 17: 225-234. PMID: 110460, DOI: 10.1016/0092-8674(79)90310-6.Peer-Reviewed Original ResearchThe 3′ terminus of 16S rRNA: secondary structure and interaction with ribosomal protein S1
Yuan R, Steitz J, Moore P, Crothers D. The 3′ terminus of 16S rRNA: secondary structure and interaction with ribosomal protein S1. Nucleic Acids Research 1979, 7: 2399-2418. PMID: 392471, PMCID: PMC342392, DOI: 10.1093/nar/7.8.2399.Peer-Reviewed Original Research
1977
3′ Terminal sequences of 16S rRNA do not explain translational specificity differences between E. coli and B. stearothermophilus ribosomes
SPRAGUE KU, STEITZ JA, GRENLEY RM, STOCKING CE. 3′ Terminal sequences of 16S rRNA do not explain translational specificity differences between E. coli and B. stearothermophilus ribosomes. Nature 1977, 267: 462-465. PMID: 327330, DOI: 10.1038/267462a0.Peer-Reviewed Original ResearchThe nucleotide sequence of a major glycine transfer RNA from the posterior silk gland of Bombyx mori L.
Zúñiga M, Steitz J. The nucleotide sequence of a major glycine transfer RNA from the posterior silk gland of Bombyx mori L. Nucleic Acids Research 1977, 4: 4175-4196. PMID: 414206, PMCID: PMC343233, DOI: 10.1093/nar/4.12.4175.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBase SequenceBombyxExocrine GlandsGlycineMolecular WeightOligoribonucleotidesRibonuclease T1RNA, Transfer
1968
Identification of the A protein as a structural component of bacteriophage R17
Steitz J. Identification of the A protein as a structural component of bacteriophage R17. Journal Of Molecular Biology 1968, 33: 923-936. PMID: 4178187, DOI: 10.1016/0022-2836(68)90328-8.Peer-Reviewed Original ResearchConceptsA proteinBacteriophage R17Amber mutantsMolecule of histidineProtein monomersProtein productsMajor polypeptidesMolecular weight estimatesStructural componentsPhage particlesR17Non-permissive hostsDefective particlesVirus particlesProteinGel filtrationHistidineCistronMutantsSpheroplastsPolypeptideHostCopiesIsolation of the A protein from bacteriophage R17
Steitz J. Isolation of the A protein from bacteriophage R17. Journal Of Molecular Biology 1968, 33: 937-945. PMID: 5700426, DOI: 10.1016/0022-2836(68)90329-x.Peer-Reviewed Original ResearchMeSH KeywordsAmino AcidsBacteriophagesChromatographyDetergentsElectrophoresisHistidineMolecular WeightTritiumViral Proteins